ID   A0A3P8SVG6_AMPPE        Unreviewed;       268 AA.
AC   A0A3P8SVG6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Protein kinase AMP-activated non-catalytic subunit beta 2 {ECO:0000313|Ensembl:ENSAPEP00000015676.1};
GN   Name=PRKAB2 {ECO:0000313|Ensembl:ENSAPEP00000015676.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000015676.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000015676.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000015676.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC       an energy sensor protein kinase that plays a key role in regulating
CC       cellular energy metabolism. In response to reduction of intracellular
CC       ATP levels, AMPK activates energy-producing pathways and inhibits
CC       energy-consuming processes: inhibits protein, carbohydrate and lipid
CC       biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC       direct phosphorylation of metabolic enzymes, and by longer-term effects
CC       via phosphorylation of transcription regulators. Also acts as a
CC       regulator of cellular polarity by remodeling the actin cytoskeleton;
CC       probably by indirectly activating myosin. Beta non-catalytic subunit
CC       acts as a scaffold on which the AMPK complex assembles, via its C-
CC       terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC       (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000256|ARBA:ARBA00025180}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010926}.
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DR   AlphaFoldDB; A0A3P8SVG6; -.
DR   STRING; 161767.ENSAPEP00000015676; -.
DR   Ensembl; ENSAPET00000016083.1; ENSAPEP00000015676.1; ENSAPEG00000011137.1.
DR   GeneTree; ENSGT00940000159284; -.
DR   OMA; IPPHKPW; -.
DR   Proteomes; UP000265080; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 6.20.250.60; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR006828; ASC_dom.
DR   InterPro; IPR037256; ASC_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR   PANTHER; PTHR10343:SF92; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; AMPKBI-like; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT   DOMAIN          178..268
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   268 AA;  29708 MW;  1430E19EE9570031 CRC64;
     MGNTSDRVSG DRHGGKAHRS DSSGSHKDQE HSSKMVDSTD DPNIFNTHGP DSKASGEKEF
     TPDLDDLVKT GPQARPTVIR WAGGGKEVYI AGSFNNWSTK IPLNKSHNDF VAILDLPEGE
     HQYKFFVDGQ WVNDPSEPVV TSQLGTINNL IQVKKSDFEV FDALQVDSLE CSDTSDLSSS
     PPGPYGQEQY VFRPEEHFKA PPILPPHLLQ VILNKDTNIS CDPALLPEPN HVMLNHLYAL
     SIKDGVMVLS ATHRYKKKYV TSLLYKPI
//